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Volumn 86, Issue 2, 2008, Pages 264-269

Structure, properties, and functions of the human small heat-shock protein HSP22 (HspB8, H11, E2IG1): A critical review

Author keywords

Congenital diseases; Phosphorylation; Small heat shock proteins

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; CHAPERONE; GLYCOLYTIC ENZYME; HEAT SHOCK PROTEIN 22; HUNTINGTIN; OLIGOMER; PROTEIN KINASE;

EID: 38849180142     PISSN: 03604012     EISSN: 10974547     Source Type: Journal    
DOI: 10.1002/jnr.21441     Document Type: Short Survey
Times cited : (58)

References (50)
  • 1
    • 0036186869 scopus 로고    scopus 로고
    • Hsp27: Novel regulator of intracellular redox state
    • Arrigo A-P. 2001. Hsp27: novel regulator of intracellular redox state. IUBMB Life 52:303-307.
    • (2001) IUBMB Life , vol.52 , pp. 303-307
    • Arrigo, A.-P.1
  • 4
    • 2642575701 scopus 로고    scopus 로고
    • Shocking degeneration
    • Benndorf R, Welsh M. 2004. Shocking degeneration. Nat Genet 36:547-548.
    • (2004) Nat Genet , vol.36 , pp. 547-548
    • Benndorf, R.1    Welsh, M.2
  • 5
    • 21244489544 scopus 로고    scopus 로고
    • HspB8, a small heat shock protein mutated in human neuromuscular disorders, has in vivo chaperone activity in cultured cells
    • Carra S, Sivilotti M, Chavez Zobel AT, Lambert H, Landry J. 2005. HspB8, a small heat shock protein mutated in human neuromuscular disorders, has in vivo chaperone activity in cultured cells. Human Mol Genet 14:1659-1669.
    • (2005) Human Mol Genet , vol.14 , pp. 1659-1669
    • Carra, S.1    Sivilotti, M.2    Chavez Zobel, A.T.3    Lambert, H.4    Landry, J.5
  • 8
    • 0038104369 scopus 로고    scopus 로고
    • Distinct chaperone mechanisms can delay the formation of aggresomes by the myopathy-causing R120G αB-crystallin mutant
    • Chavez Zobel AT, Loranger A, Marceau N, Theriault JR, Lambert H, Landry J. 2003. Distinct chaperone mechanisms can delay the formation of aggresomes by the myopathy-causing R120G αB-crystallin mutant. Human Mol Genet 12:1609-1620.
    • (2003) Human Mol Genet , vol.12 , pp. 1609-1620
    • Chavez Zobel, A.T.1    Loranger, A.2    Marceau, N.3    Theriault, J.R.4    Lambert, H.5    Landry, J.6
  • 9
    • 3242776825 scopus 로고    scopus 로고
    • Mammahan Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity
    • Chowdary TK, Raman B, Ramakrishna T, Rao CH. 2004. Mammahan Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity. Biochem J 381:379-387.
    • (2004) Biochem J , vol.381 , pp. 379-387
    • Chowdary, T.K.1    Raman, B.2    Ramakrishna, T.3    Rao, C.H.4
  • 10
  • 11
    • 0027472047 scopus 로고
    • Evolution of the α-crystallin/small heat-shock protein family
    • De Jong WW, Leunissen JAM, Voorter CEM. 1993. Evolution of the α-crystallin/small heat-shock protein family. Mol Biol Evol 10:103-126.
    • (1993) Mol Biol Evol , vol.10 , pp. 103-126
    • De Jong, W.W.1    Leunissen, J.A.M.2    Voorter, C.E.M.3
  • 16
    • 0037359564 scopus 로고    scopus 로고
    • The sperm outer dense fiber protein is the 10th member of the superfamily of mammalian small heat shock proteins
    • Fontaine JM, Rest JS, Welsh MJ, Benndorf R. 2003. The sperm outer dense fiber protein is the 10th member of the superfamily of mammalian small heat shock proteins. Cell Stress Chaperone 8:62-69.
    • (2003) Cell Stress Chaperone , vol.8 , pp. 62-69
    • Fontaine, J.M.1    Rest, J.S.2    Welsh, M.J.3    Benndorf, R.4
  • 19
    • 14144255401 scopus 로고    scopus 로고
    • Insights into the domains required for dimerization and assembly of human alphaB crystallin
    • Ghosh JG, Clark JI. 2005. Insights into the domains required for dimerization and assembly of human alphaB crystallin. Protein Sci 14:684-695.
    • (2005) Protein Sci , vol.14 , pp. 684-695
    • Ghosh, J.G.1    Clark, J.I.2
  • 20
    • 0141844530 scopus 로고    scopus 로고
    • Forced expression of the H11 heat shock protein can be regulated by DNA methylation and trigger apoptosis in human cells
    • Gober MD, Smith CC, Ueda K, Toretsky JA, Aurehan L. 2003. Forced expression of the H11 heat shock protein can be regulated by DNA methylation and trigger apoptosis in human cells. J Biol Chem 278:37600-37609.
    • (2003) J Biol Chem , vol.278 , pp. 37600-37609
    • Gober, M.D.1    Smith, C.C.2    Ueda, K.3    Toretsky, J.A.4    Aurehan, L.5
  • 21
    • 21344465226 scopus 로고    scopus 로고
    • Herpes simplex virus type 2 encodes a heat shock proteins homologue with apoptosis regulatory function
    • Gober MD, Wales SQ, Aurelian L. 2005. Herpes simplex virus type 2 encodes a heat shock proteins homologue with apoptosis regulatory function. Frontiers Bioscienses 10:2788-2803.
    • (2005) Frontiers Bioscienses , vol.10 , pp. 2788-2803
    • Gober, M.D.1    Wales, S.Q.2    Aurelian, L.3
  • 22
    • 0034724559 scopus 로고    scopus 로고
    • Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies
    • Haley DA, Bova MP, Huang QL, Mchaourab HS, Stewart PL. 2000. Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies. J Mol Biol 298:261-272.
    • (2000) J Mol Biol , vol.298 , pp. 261-272
    • Haley, D.A.1    Bova, M.P.2    Huang, Q.L.3    Mchaourab, H.S.4    Stewart, P.L.5
  • 23
    • 20544446917 scopus 로고    scopus 로고
    • H11 has dose-dependent and dual hypertrophic and proapoptotic functions in cardiac myocytes
    • Hase M, Depre C, Vatner SF, Sadoshima J. 2005. H11 has dose-dependent and dual hypertrophic and proapoptotic functions in cardiac myocytes. Biochem J 388:475-483.
    • (2005) Biochem J , vol.388 , pp. 475-483
    • Hase, M.1    Depre, C.2    Vatner, S.F.3    Sadoshima, J.4
  • 24
    • 27144448839 scopus 로고    scopus 로고
    • Some like it hot: The structure and function of small heat-shock proteins
    • Haslbeck M, Franzmann T, Weinfurtner D, Buchner J. 2005. Some like it hot: the structure and function of small heat-shock proteins. Nat Struct Mol Biol 12:842-846.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 842-846
    • Haslbeck, M.1    Franzmann, T.2    Weinfurtner, D.3    Buchner, J.4
  • 25
    • 34547464698 scopus 로고    scopus 로고
    • Structure, function, properties and role in neurological diseases and other diseases of sHsp22
    • doi 10.1002/jnr.21231
    • Hu Z, Chen L, Zhang J, Li T, Tang J, Xu N, Wang X. 2007. Structure, function, properties and role in neurological diseases and other diseases of sHsp22. J Neurosci Res doi 10.1002/jnr.21231
    • (2007) J Neurosci Res
    • Hu, Z.1    Chen, L.2    Zhang, J.3    Li, T.4    Tang, J.5    Xu, N.6    Wang, X.7
  • 27
    • 0037358061 scopus 로고    scopus 로고
    • Kappe G, Franck E.Verschuure P.Boelens WC, Leunissen JAM, de Jong WW. 2003. The human genome encodes 10 α-crystallin-related small heat shock proteins: HspB1-10. Cell Stress Chaperones 8:53-61.
    • Kappe G, Franck E.Verschuure P.Boelens WC, Leunissen JAM, de Jong WW. 2003. The human genome encodes 10 α-crystallin-related small heat shock proteins: HspB1-10. Cell Stress Chaperones 8:53-61.
  • 29
    • 33748892808 scopus 로고    scopus 로고
    • Structure and properties of K141E mutant of small heat shock proteins HSP22 (HspB8, H11) that is expressed in human neuromuscular disorders
    • Kim MV, Kasakov AS, Seit-Nebi AS, Marston SB, Gusev NB. 2006. Structure and properties of K141E mutant of small heat shock proteins HSP22 (HspB8, H11) that is expressed in human neuromuscular disorders. Arch Biochem Biophys 454:32-41.
    • (2006) Arch Biochem Biophys , vol.454 , pp. 32-41
    • Kim, M.V.1    Kasakov, A.S.2    Seit-Nebi, A.S.3    Marston, S.B.4    Gusev, N.B.5
  • 30
    • 8444231226 scopus 로고    scopus 로고
    • The problem of protein kinase activity of small heat shock protein Hsp22 (H11 or HspB8)
    • Kim MV, Seit-Nebi AS, Gusev NB. 2004a. The problem of protein kinase activity of small heat shock protein Hsp22 (H11 or HspB8). Biochem Biophys Res Commun 325:649-652.
    • (2004) Biochem Biophys Res Commun , vol.325 , pp. 649-652
    • Kim, M.V.1    Seit-Nebi, A.S.2    Gusev, N.B.3
  • 32
    • 0031916707 scopus 로고    scopus 로고
    • The R1 subunit of herpes simplex virus ribonucleotide reductase is a good substrate for host protein kinase but is not itself a protein kinase
    • Langelier Y, Champoux L, Hamel M, Guilbault C, Lamarche N, Gaudreau P, Massie B. 1998. The R1 subunit of herpes simplex virus ribonucleotide reductase is a good substrate for host protein kinase but is not itself a protein kinase. J Biol Chem 273:1435-1443.
    • (1998) J Biol Chem , vol.273 , pp. 1435-1443
    • Langelier, Y.1    Champoux, L.2    Hamel, M.3    Guilbault, C.4    Lamarche, N.5    Gaudreau, P.6    Massie, B.7
  • 34
    • 0034613387 scopus 로고    scopus 로고
    • The small heat shock protein Hsp22 of Drosophila melanogaster is a mitochondrial protein displaying oligomeric organization
    • Morrow G, Inaguma Y, Kato K, Tanguay RM. 2000. The small heat shock protein Hsp22 of Drosophila melanogaster is a mitochondrial protein displaying oligomeric organization. J Biol Chem 275:31204-31210.
    • (2000) J Biol Chem , vol.275 , pp. 31204-31210
    • Morrow, G.1    Inaguma, Y.2    Kato, K.3    Tanguay, R.M.4
  • 35
    • 33644842178 scopus 로고    scopus 로고
    • Difference in the chaperone-like activities of the four main small heat shock proteins of Drosophila melanogaster
    • Morrow G, Heikkila JJ, Tanguay RM. 2006. Difference in the chaperone-like activities of the four main small heat shock proteins of Drosophila melanogaster. Cell Stress Chaperones 11:51-60.
    • (2006) Cell Stress Chaperones , vol.11 , pp. 51-60
    • Morrow, G.1    Heikkila, J.J.2    Tanguay, R.M.3
  • 36
    • 2442649342 scopus 로고    scopus 로고
    • Overexpression of the small mitochondrial Hsp22 extends Drosophila life span and increases resistance to oxidative stress
    • Morrow G, Samson M, Michaud S, Tanguay RM. 2004. Overexpression of the small mitochondrial Hsp22 extends Drosophila life span and increases resistance to oxidative stress. FASEB J 18:598-599.
    • (2004) FASEB J , vol.18 , pp. 598-599
    • Morrow, G.1    Samson, M.2    Michaud, S.3    Tanguay, R.M.4
  • 37
    • 0036195722 scopus 로고    scopus 로고
    • α-Crystallin-type heat shock proteins: Socializing minichaperones in the context of a multichaperone network
    • Narberhaus F. 2002. α-Crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network. Microbiol Mol Biol Rev 66:64-93.
    • (2002) Microbiol Mol Biol Rev , vol.66 , pp. 64-93
    • Narberhaus, F.1
  • 39
    • 0034682806 scopus 로고    scopus 로고
    • A novel human gene similar to the protein kinase (PK) coding domain of the large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10) codes for a serine-threonine PK and is expressed in melanoma cells
    • Smith CC, Yu YX, Kulka M, Aurelian L. 2000. A novel human gene similar to the protein kinase (PK) coding domain of the large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10) codes for a serine-threonine PK and is expressed in melanoma cells. J Biol Chem 275:25690-25699.
    • (2000) J Biol Chem , vol.275 , pp. 25690-25699
    • Smith, C.C.1    Yu, Y.X.2    Kulka, M.3    Aurelian, L.4
  • 40
    • 0038043235 scopus 로고    scopus 로고
    • Analysis of the interaction of small heat shock proteins with unfolding proteins
    • Stromer T, Ehrnsperger M, Gaestel M, Buchner J. 2003. Analysis of the interaction of small heat shock proteins with unfolding proteins. J Biol Chem 278:18015-18021.
    • (2003) J Biol Chem , vol.278 , pp. 18015-18021
    • Stromer, T.1    Ehrnsperger, M.2    Gaestel, M.3    Buchner, J.4
  • 42
    • 33644847834 scopus 로고    scopus 로고
    • Conformational changes resulting from pseudophosphorylation of mammalian small heat shock proteins - a two-hybrid study
    • Sun X, Welsh MJ, Benndorf R. 2006. Conformational changes resulting from pseudophosphorylation of mammalian small heat shock proteins - a two-hybrid study. Cell Stress Chaperones 11:71-70.
    • (2006) Cell Stress Chaperones , vol.11 , pp. 71-70
    • Sun, X.1    Welsh, M.J.2    Benndorf, R.3
  • 43
    • 20444478694 scopus 로고    scopus 로고
    • The small heat shock proteins and their role in human disease
    • Sun Y, MacRae TH. 2005. The small heat shock proteins and their role in human disease. FEBS J 272:2613-2627.
    • (2005) FEBS J , vol.272 , pp. 2613-2627
    • Sun, Y.1    MacRae, T.H.2
  • 44
    • 19944433659 scopus 로고    scopus 로고
    • Tang BS, Zhao GH, Luo W, Xia K, Cai F, Pan Q, Zhang RX, Zhang FF, Liu XM, Chen B, Zhang C.Shen L, Jiang H, Long ZG, Dai H. 2005. Small heat shock protein 22 mutated in autosomal dominant Charcot-Marie-Tooth disease type 2L. Hum Genet 116:222-224.
    • Tang BS, Zhao GH, Luo W, Xia K, Cai F, Pan Q, Zhang RX, Zhang FF, Liu XM, Chen B, Zhang C.Shen L, Jiang H, Long ZG, Dai H. 2005. Small heat shock protein 22 mutated in autosomal dominant Charcot-Marie-Tooth disease type 2L. Hum Genet 116:222-224.
  • 45
    • 2542451125 scopus 로고    scopus 로고
    • Essential role of the NH2-terminal WD/EPF motif in the phosphorylation-activated protective function of mammalian Hsp27
    • Theriault JR, Lambert H, Chavez-Zobel AT, Charest G, Lavigne P, Landry J. 2004. Essential role of the NH2-terminal WD/EPF motif in the phosphorylation-activated protective function of mammalian Hsp27. J Biol Chem 279:23463-23471.
    • (2004) J Biol Chem , vol.279 , pp. 23463-23471
    • Theriault, J.R.1    Lambert, H.2    Chavez-Zobel, A.T.3    Charest, G.4    Lavigne, P.5    Landry, J.6
  • 46
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: Intrinsically disorder as an ID for recognition, regulation and cell signaling
    • Uversky VN, Oldfield C, Dunker AK. 2005. Showing your ID: intrinsically disorder as an ID for recognition, regulation and cell signaling. J Mol Recognit 18:343-384.
    • (2005) J Mol Recognit , vol.18 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.2    Dunker, A.K.3
  • 47
    • 0242407366 scopus 로고    scopus 로고
    • Expression of small heat shock proteins HspB2, HspB8, Hsp20 and cvHsp in different tissues of the perinatal developing pig
    • Verschuure P, Tatard C, Boelens WC, Grognet J-F, David JC. 2003. Expression of small heat shock proteins HspB2, HspB8, Hsp20 and cvHsp in different tissues of the perinatal developing pig. Eur J Cell Biol 82:523-530.
    • (2003) Eur J Cell Biol , vol.82 , pp. 523-530
    • Verschuure, P.1    Tatard, C.2    Boelens, W.C.3    Grognet, J.-F.4    David, J.C.5
  • 48
    • 16644375829 scopus 로고    scopus 로고
    • Increased expression of H11 kinase stimulated glycogen synthesis in the heart
    • Wang L, Zajac A, Hedhli N, Depre C. 2004. Increased expression of H11 kinase stimulated glycogen synthesis in the heart. Mol Cel Biochem. 265:71-87.
    • (2004) Mol Cel Biochem , vol.265 , pp. 71-87
    • Wang, L.1    Zajac, A.2    Hedhli, N.3    Depre, C.4
  • 49
    • 33646190092 scopus 로고    scopus 로고
    • Wilhelmus MMM, Boelens WC, Otte-Holler I, Kamps B, Kusters B, Maat-Scheman MLC, de Waal RMW, Verbeek MM. 2006. Small heat shock protein HspB8: its distribution in Alzheimer's diseases brains and its inhibition of amyloid-β protein aggregation and cerebrovascular amyloid-β toxicity. Acta Neuropathol (Berl) 111:1390143.
    • Wilhelmus MMM, Boelens WC, Otte-Holler I, Kamps B, Kusters B, Maat-Scheman MLC, de Waal RMW, Verbeek MM. 2006. Small heat shock protein HspB8: its distribution in Alzheimer's diseases brains and its inhibition of amyloid-β protein aggregation and cerebrovascular amyloid-β toxicity. Acta Neuropathol (Berl) 111:1390143.
  • 50
    • 33846222825 scopus 로고    scopus 로고
    • Identification of cyclinD1 and estrogen-regulated genes contributing to breast carcinogenesis and progression
    • Yang C, Trent S, Ionescu-Tiba V, Lan L, Shioda T, Sgroi D, Schmidt EV. 2006. Identification of cyclinD1 and estrogen-regulated genes contributing to breast carcinogenesis and progression. Cancer Res 66:11649-11658.
    • (2006) Cancer Res , vol.66 , pp. 11649-11658
    • Yang, C.1    Trent, S.2    Ionescu-Tiba, V.3    Lan, L.4    Shioda, T.5    Sgroi, D.6    Schmidt, E.V.7


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